ID   A0A140D7R9_PASMD        Unreviewed;       931 AA.
AC   A0A140D7R9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:AMK08943.1};
GN   ORFNames=NM948_00755 {ECO:0000313|EMBL:MDA5622095.1};
OS   Pasteurella multocida.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=747 {ECO:0000313|EMBL:AMK08943.1};
RN   [1] {ECO:0000313|EMBL:AMK08943.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UNMSM {ECO:0000313|EMBL:AMK08943.1};
RA   Maturrano L., Hurtado R., Allasi N., Juscamayta E., Fernandez D.,
RA   Maximiliano J., Rimac R., Rosadio R.;
RT   "Draft genome sequence of Pasteurella multocida isolated from alpaca
RT   pneumonia.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MDA5622095.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIVEDIPm19 {ECO:0000313|EMBL:MDA5622095.1};
RA   Prajapati A., Yogisharadhya R., Mohanty N., Chanda M., Mendem S.K.,
RA   Siddaramappa S., Shivachandra S.B.;
RT   "Genome-based characterization of novel serogroup A variants of Pasteurella
RT   multocida.";
RL   Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; KP661104; AMK08943.1; -; Genomic_DNA.
DR   EMBL; JANJHC010000001; MDA5622095.1; -; Genomic_DNA.
DR   RefSeq; WP_014326191.1; NZ_SJDX01000007.1.
DR   KEGG; pmul:DR93_1783; -.
DR   PATRIC; fig|747.135.peg.1733; -.
DR   Proteomes; UP001145481; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:MDA5622095.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          591..784
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   931 AA;  105634 MW;  473863747B54CCA0 CRC64;
     MQKNTPISEW LTSSALGGTN QSYIEELYED YLRDPDSVDA SWQTIFNALP KSHTAVEQPH
     SQVRDYFKRL ARDNSPNGVS VIDPNVSARL VKLLAYVNAH RNRGHLHADL DPLNLWQRMD
     APTLDYKYHG FTESDLDETF DLGGEVAHRN QISLRELQDL LQKTYCGTIG LEFMHVNDVE
     ARTWLQNKLE SRVTQGFNKE EQLKFLEELT AADGLERYLG AKFPGAKRFS LEGSDSFILL
     MKEIVRHGKR NGIDEIAMGM AHRGRLNMLV NVLGKKPSEL FDEFAGKHNG NGTGDVKYHQ
     GFSSDFMTDD GIVHLVLAFN PSHLEIVSPV VIGSVRARQK RINDHEKAKV LPVTVHGDSA
     VIGQGVVQET LNMSGTRGYS VGGTIRIVIN NQIGFTTSNP HDTRSTEYCT DIAKMIEAPV
     IHVNGDDPEA VAYAARMAVE YRTLFKRDIF IDLVSYRRHG HNEADEPSAT QPLMYDRIKK
     HPTPRKVYAD RLIAQGVINE EAATELVNNY RDALDRGDCV VAEWREMDLT TKDWTKYLSR
     EWCEYESKFD AARFKGLAQK VCEYPAQHEL HSRVNKIYAD RTLMANGEKL FDWGMAETMA
     YATLLDEGYH VRLSGEDAGR GTFFHRHSVL HNQKDATLYI PLANLHGSQG RFEVWDSVLT
     ENAVLAFEYG YATTDPKTLT IWEAQFGDFA NCAQVVVDQF ISSGEQKWGR MCGLVMLLPH
     GYEGQGPEHS SARLERYLQL CAQQNMQVCV PSTPAQIYHL LRRQMIRKVR RPLVVISPKS
     LLRHPLAVST MEELIDGKFQ NVIPEVDALD PKHVRRVVMC SGKVYYDLLE QRRKNNQSDV
     AIIRIEQLYP YPHEEMKQIL ADYSHVTDYV WCQEEPLNQG AWYCSQHNFV SSIPEHGKLR
     YVGRPASASP AVGYMSLHNE QQTALVNEAL A
//